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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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The interaction of phospholipase C-beta 3 with Shank2 regulates mGluR-mediated calcium signal

Cited 53 times inthomson ciCited 55 times inthomson ci
Title
The interaction of phospholipase C-beta 3 with Shank2 regulates mGluR-mediated calcium signal
Author
Hwang, Jong-IkKim, Hyeon SooLee, Jae RanKim, EunjoonRyu, Sung HoSuh, Pann-Ghill
Keywords
Biochemistry; Biological membranes; Calcium; Molecular biology; Scaffolds
Issue Date
2005-04
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.280, no.13, pp.12467 - 12473
Abstract
Phospholipase C-beta isozymes that are activated by G protein-coupled receptors ( GPCR) and heterotrimeric G proteins carry a PSD-95/Dlg/ZO-1 (PDZ) domain binding motif at their C terminus. Through interactions with PDZ domains, this motif may endow the PLC-beta isozyme with specific roles in GPCR signaling events that occur in compartmentalized regions of the plasma membrane. In this study, we identified the interaction of PLC-beta 3 with Shank2, a PDZ domain-containing multimodular scaffold in the postsynaptic density (PSD). The C terminus of PLC-beta 3, but not other PLC-beta isotypes, specifically interacts with the PDZ domain of Shank2. Homer 1b, a Shank-interacting protein that is linked to group I metabotropic glutamate receptors and IP3 receptors, forms a multiple complex with Shank2 and PLC-beta 3. Importantly, microinjection of a synthetic peptide specifically mimicking the C terminus of PLC-beta 3 markedly reduces the mGluR-mediated intracellular calcium response. These results demonstrate that Shank2 brings PLC-beta 3 closer to Homer 1b and constitutes an efficient mGluR-coupled signaling pathway in the PSD region of neuronal synapses
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DOI
10.1074/jbc.M410740200
ISSN
0021-9258
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BME_Journal Papers
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